ID   BMNL3_BOMOR             Reviewed;         200 AA.
AC   P29004;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   18-SEP-2019, entry version 58.
DE   RecName: Full=Bombinin-like peptides 3;
DE   Contains:
DE     RecName: Full=Acidic peptide 1;
DE   Contains:
DE     RecName: Full=Bombinin-like peptide 3;
DE              Short=BLP-3;
DE   Contains:
DE     RecName: Full=Octapeptide 1;
DE   Contains:
DE     RecName: Full=Acidic peptide 2;
DE   Contains:
DE     RecName: Full=Octapeptide 2;
DE   Contains:
DE     RecName: Full=Acidic peptide 3;
DE   Contains:
DE     RecName: Full=GH-1 peptide;
DE   Flags: Precursor;
OS   Bombina orientalis (Oriental fire-bellied toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=8346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 44-68 AND
RP   105-129, AND AMIDATION AT PHE-68 AND PHE-129.
RC   TISSUE=Skin, and Skin secretion;
RX   PubMed=1744108;
RA   Gibson B.W., Tang D., Mandrell R., Kelly M., Spindel E.R.;
RT   "Bombinin-like peptides with antimicrobial activity from skin
RT   secretions of the Asian toad, Bombina orientalis.";
RL   J. Biol. Chem. 266:23103-23111(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=9684858; DOI=10.1016/s0014-5793(98)00718-2;
RA   Miele R., Ponti D., Boman H.G., Barra D., Simmaco M.;
RT   "Molecular cloning of a bombinin gene from Bombina orientalis:
RT   detection of NF-kappaB and NF-IL6 binding sites in its promoter.";
RL   FEBS Lett. 431:23-28(1998).
CC   -!- FUNCTION: Has antimicrobial activity, but no hemolytic activity.
CC       Preference on killing Gram-negative non-enteric bacteria.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the bombinin family. {ECO:0000305}.
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DR   EMBL; M76484; AAA73095.1; -; Genomic_DNA.
DR   EMBL; AJ007445; CAA07511.1; -; Genomic_DNA.
DR   PIR; C41575; C41575.
DR   SMR; P29004; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR007962; Bombinin.
DR   Pfam; PF05298; Bombinin; 2.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     16       Or 18.
FT   PEPTIDE      17     43       Acidic peptide 1. {ECO:0000255}.
FT                                /FTId=PRO_0000003059.
FT   PEPTIDE      44     68       Bombinin-like peptide 3.
FT                                /FTId=PRO_0000003060.
FT   PEPTIDE      72     79       Octapeptide 1. {ECO:0000255}.
FT                                /FTId=PRO_0000003061.
FT   PEPTIDE      82    104       Acidic peptide 2. {ECO:0000255}.
FT                                /FTId=PRO_0000003062.
FT   PEPTIDE     105    129       Bombinin-like peptide 3.
FT                                /FTId=PRO_0000003063.
FT   PEPTIDE     133    140       Octapeptide 2. {ECO:0000255}.
FT                                /FTId=PRO_0000003064.
FT   PEPTIDE     143    177       Acidic peptide 3. {ECO:0000255}.
FT                                /FTId=PRO_0000003065.
FT   PEPTIDE     183    200       GH-1 peptide. {ECO:0000255}.
FT                                /FTId=PRO_0000003066.
FT   MOD_RES      68     68       Phenylalanine amide.
FT                                {ECO:0000269|PubMed:1744108}.
FT   MOD_RES     129    129       Phenylalanine amide.
FT                                {ECO:0000269|PubMed:1744108}.
FT   CONFLICT     11     11       I -> F (in Ref. 2; CAA07511).
FT                                {ECO:0000305}.
FT   CONFLICT     84     84       A -> V (in Ref. 2; CAA07511).
FT                                {ECO:0000305}.
FT   CONFLICT     87     87       H -> Q (in Ref. 2; CAA07511).
FT                                {ECO:0000305}.
FT   CONFLICT    139    139       M -> V (in Ref. 2; CAA07511).
FT                                {ECO:0000305}.
FT   CONFLICT    162    162       M -> R (in Ref. 2; CAA07511).
FT                                {ECO:0000305}.
FT   CONFLICT    166    166       S -> D (in Ref. 2; CAA07511).
FT                                {ECO:0000305}.
FT   CONFLICT    172    178       Missing (in Ref. 2; CAA07511).
FT                                {ECO:0000305}.
FT   CONFLICT    184    184       L -> I (in Ref. 2; CAA07511).
FT                                {ECO:0000305}.
FT   CONFLICT    187    187       I -> V (in Ref. 2; CAA07511).
FT                                {ECO:0000305}.
FT   CONFLICT    192    200       SNALGGLLG -> GKPLESLLE (in Ref. 2;
FT                                CAA07511). {ECO:0000305}.
SQ   SEQUENCE   200 AA;  21934 MW;  1185F0836BF8A277 CRC64;
     MNFKYIVAVS ILIASAYARS EENDIQSLSQ RDVLEEESLR EIRGIGAAIL SAGKSALKGL
     AKGLAEHFGK RTAEDHEVMK RLEAAIHSLS QRDVLEEESL REIRGIGAAI LSAGKSALKG
     LAKGLAEHFG KRTAEEHEMM KRLEAVMRDL DSLDYPEEAS EMETRSFNQE EIANLYTKKE
     KRILGPILGL VSNALGGLLG
//